CN110343146B - Hypsizygus marmoreus flavor-developing peptide and preparation method and application thereof - Google Patents
Hypsizygus marmoreus flavor-developing peptide and preparation method and application thereof Download PDFInfo
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- CN110343146B CN110343146B CN201910628396.7A CN201910628396A CN110343146B CN 110343146 B CN110343146 B CN 110343146B CN 201910628396 A CN201910628396 A CN 201910628396A CN 110343146 B CN110343146 B CN 110343146B
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
- A23L27/20—Synthetic spices, flavouring agents or condiments
- A23L27/21—Synthetic spices, flavouring agents or condiments containing amino acids
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
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Abstract
The invention provides a hypsizygus marmoreus flavor-developing peptide and a preparation method and application thereof. The hypsizygus marmoreus taste-presenting peptide is characterized in that the amino acid sequence of the hypsizygus marmoreus taste-presenting peptide is shown in SEQ ID NO: 1 is shown. The Hypsizygus marmoreus disclosed by the invention is tasty and delicious in taste peptide, and brings a thick taste effect when added into food. The research of the invention finds that the Maillard peptide obtained by using the Hypsizygus marmoreus taste peptide prepared by the embodiment to carry out Maillard reaction has good flavor enhancement effect.
Description
Technical Field
The invention belongs to the field of dietetics, relates to a seasoning, and particularly relates to a hypsizygus marmoreus flavor-presenting peptide.
Background
The richness sensation is the sixth taste sensation in addition to the five basic tastes (sour, sweet, bitter, salty, umami), which was first discovered and named by japanese scientists. The thickening peptide is a substance capable of increasing the overall thickening effect of food, and is named as kokumi peptide. Unlike umami, a rich taste is not a clearly perceptible taste, which mostly refers to a sensation: after the kokumi peptide is added, the food becomes more delicious, the thick feeling is stronger, the food has more taste, and the like. Peptides are most of the substances with kokumi taste. The Kokumi peptide is generally similar to umami taste when dissolved in water, and when present with salt or sodium glutamate, it can significantly reduce the salt and sodium glutamate threshold, which can also be referred to as a taste enhancer. The Kokumi peptide does not affect the taste of the food itself since it does not have a noticeable taste by itself.
Food taste research scientists have found that the taste of foods is diverse in exploring the principles of food taste presentation. These flavors are first stimulated and sensed by taste-sensitive receptors on the various taste buds and then transmitted to the brain nerve center of the human body through specific conduction pathways. The perception of taste by humans is generally divided into 3 stages: front, middle and back. The food added with the kokumi peptide has more round and natural taste in the front section, softer and thicker middle section and longer aftertaste in the rear section.
Studies find that the thick sensory peptide can stimulate CaSR calcium sensitive receptors. Can excite the calcium sensitive receptor of human body and modify the basic taste of sour, sweet, bitter, salty and fresh etc. Recent studies have shown that the profuse sensory peptide is perceived by specific calcium-sensitive receptors. The multiple flavor-developing polypeptides have a synergistic effect together, and different calcium sensitive receptors have complex perception, so that the sweet taste is sweeter, the salty taste is more salty, and the overall taste perception is increased.
Hypsizygus marmoreus (Hypsizygus marmoreus) belonging to Basidiomycotina, Agaricaceae, Agaricales, Lyophyllaceae, Hypsizygus is an excellent edible fungus in northern temperate zone, is grey white, covered with hemisphere, covered with light brown hidden mark in the center, tender in meat quality, has thick seafood crab taste, and has high yield. Hypsizygus marmoreus contains abundant polysaccharides, vitamins and amino acids. Fresh mushrooms are thick and heavy, relatively hard to touch, light in weight and high in moisture content. The research on the Hypsizygus marmoreus at the present stage mainly focuses on the cultivation aspect of the Hypsizygus marmoreus, and rarely reports on the research on the flavor-presenting peptide. However, practical tests show that the dried Hypsizygus marmoreus contains more protein than other varieties, and is 26.81%, so that the extraction of flavor peptides from Hypsizygus marmoreus is feasible.
Disclosure of Invention
The invention aims to provide a hypsizygus marmoreus flavor development peptide and a preparation method and application thereof.
In order to achieve the purpose, the invention provides a hypsizygus marmoreus taste-presenting peptide which is characterized in that the amino acid sequence of the hypsizygus marmoreus taste-presenting peptide is shown as SEQ ID NO: 1 is shown.
The invention also provides a preparation method of the hypsizygus marmoreus taste-presenting peptide, which is characterized by comprising the following steps of:
step 1: extracting water soluble components from Hypsizygus marmoreus by high pressure cooking;
step 2: intercepting components with molecular weight of 500Da to 3000Da by ultrafiltration membrane separation method;
and step 3: and (3) carrying out chromatography and high performance liquid separation and purification on the obtained membrane separation component to obtain the hypsizygus marmoreus taste peptide with the amino acid sequence of SEQ ID NO. 1.
Preferably, the high pressure cooking conditions in step 1 are as follows: cleaning Hypsizygus marmoreus, adding water, homogenizing, steaming under 35-45 kPa for 1.5-3.5 h, filtering, centrifuging, and collecting supernatant.
Preferably, the chromatography in step 3 is gel chromatography.
Preferably, the Hypsizygus marmoreus taste peptide is identified by UPLC-Q-TOF-MS.
The invention also provides application of the hypsizygus marmoreus taste-presenting peptide in food.
The invention also provides a food which is characterized by containing the crab-flavored mushroom flavor-developing peptide.
Preferably, the food is a seasoning.
The invention also provides a Hypsizygus marmoreus Maillard peptide prepared by carrying out Maillard reaction on the Hypsizygus marmoreus flavor-developing peptide.
The Hypsizygus marmoreus flavor-developing peptide is derived from a Hypsizygus marmoreus extract. In a specific embodiment of the invention, after the ultrafiltration fraction is chromatographed, the fraction with the strongest thickening effect is selected by artificial sensory evaluation, and the fraction is chromatographed by Sephadex G-15 gel chromatography. And adding the chromatographic components into the chicken soup, and selecting the component with the thickest feeling through artificial sensory evaluation. Preferably, RP-HPLC method is used for separation and purification. Preferably, the structure is identified by UPLC-Q-TOF-MS.
The invention firstly obtains water-soluble components from the hypsizygus marmoreus by high-pressure cooking, and then carries out membrane separation on the water-soluble components for further separation and purification. The hypsizygus marmoreus flavor peptide of the invention is used as one of flavor development substances in the field of foods, such as base materials or auxiliary materials for food seasonings, which are conventional applications of flavor development substances.
Compared with the prior art, the invention has remarkable technical progress. The Hypsizygus marmoreus disclosed by the invention is tasty and delicious in taste peptide, and brings a thick taste effect when added into food. The research of the invention finds that the Maillard peptide obtained by using the Hypsizygus marmoreus taste peptide prepared by the embodiment to carry out Maillard reaction has good flavor enhancement effect.
Drawings
FIG. 1 is a chromatographic spectrum of a membrane separation component with the molecular weight of 500Da-3000Da after Sephadex G-15 gel chromatography separation.
FIG. 2 shows the taste dilution analysis results of the membrane separation fraction P2 and the chromatographic fractions F1-F6.
FIG. 3 shows the results of taste intensity of chromatography fractions F1-F6 in chicken broth.
FIG. 4 is an RP-HPLC separation spectrum of chromatographic fraction F4.
FIG. 5 shows the results of the taste intensity of three components F4a, F4b and F4c in chicken broth.
FIG. 6 is a time of flight mass spectrometry (TOF MS) first order mass spectrum of component F4 b;
FIG. 7 is a time-of-flight mass spectrometry (TOF MS) second order mass spectrum of the F4b component.
Detailed Description
The invention will be further illustrated with reference to the following specific examples. It should be understood that these examples are for illustrative purposes only and are not intended to limit the scope of the present invention. Further, it should be understood that various changes or modifications of the present invention may be made by those skilled in the art after reading the teaching of the present invention, and such equivalents may fall within the scope of the present invention as defined in the appended claims.
Example 1
A preparation method of hypsizygus marmoreus taste-presenting peptide comprises the following specific steps:
step (1): preparation of Hypsizygus marmoreus water-soluble extract
Raw materials: hypsizygus marmoreus was purchased from Shanghai Fengchi Biotech Co. Cleaning Hypsizygus marmoreus, removing impurities, adding water, homogenizing with a homogenizer, adding deionized water at a ratio of 1:1, and steaming under 40kPa for 120 min. Filtering with double-layer gauze, centrifuging the filtrate at 4 deg.C at 10000r for 10min, and collecting supernatant.
Step (2): separation and purification of crab-flavor mushroom thick peptide extract
Ultrafiltering the supernatant obtained in the last step by using ultrafiltration membranes with molecular weight cut-off ranges of 3000Da and 500Da, collecting ultrafiltration components (marked as P1, P2 and P3) with molecular weights of less than 500Da, 500-3000Da and more than 3000Da, freeze-drying and storing in a refrigerator at the temperature of-20 ℃.
The membrane separation fraction P2 (lyophilized sample powder) was prepared into a solution with a concentration of 25mg/ml, and further chromatographically separated by Sephadex G-15 gel chromatography with ultrapure water as an eluent at an elution flow rate of 0.9 ml/min. The chromatogram results are shown in FIG. 1, with the abscissa representing the elution time (min) and the ordinate representing the abundance at a detection wavelength of 220 nm. From fig. 1, 6 absorption peaks can be seen, that is, 6 separated components are obtained by chromatography, and 6 chromatography components (sequentially represented by F1, F2, F3, F4, F5 and F6) obtained in the elution process are collected. Freeze-drying, and storing the freeze-dried sample powder at-20 deg.C.
And (3): the taste characteristics of the ultrafiltration fraction P2 and the chromatography fractions F1-F6 were analyzed using artificial sensory evaluation analysis.
The sensory evaluation method adopts a Taste Dilution Analysis (TDA) method to determine the dilution factors of each component obtained by gel separation and the membrane separation component P2, and comprises the following specific operations: taking freeze-dried component samples of P2 and F1-F6 respectively to prepare 25mg/ml solutions, gradually diluting the solutions by deionized water in a ratio of 1:1 to prepare a series of solutions with concentration gradients, and evaluating each dilution level by a three-point test until taste cannot be tasted by a certain dilution factor. The dilution factor (TD) is recorded. Sensory evaluation persons were 8 persons (4 men and 4 women, aged 25 to 30 years), and before sensory analysis, sensory analysis panelists were trained with 1% sucrose solution as a sweet taste standard, 0.35% sodium chloride solution as a salty taste standard, 0.08% quinine solution as a bitter taste standard, 0.35% sodium glutamate solution as an umami taste standard, and 0.08% citric acid solution as an acidic taste standard. Sipping at 9:00am-12:00am daily for five days to train their taste senses. The dilution factor when the flavor difference between a certain dilution level solution and two deionized water is just identified is the flavor intensity dilution factor, namely the TD value. The TD value is the average value of the evaluation results of each sensory evaluator, and each sample is evaluated at normal temperature after being repeated three times in different time. Each sensory evaluator also required a descriptive sensory evaluation of the taste profile of each sample in water.
The results of the flavor intensity dilution factors of the membrane separation fraction P2 and the chromatographic fractions F1-F6 are shown in FIG. 2, in which the abscissa represents the fraction names and the ordinate represents the flavor intensity dilution factors of the respective fractions.
As can be seen from FIG. 2, the TD values of the membrane separation fraction P2 and the chromatography fraction F4 were the highest, and the taste was the strongest in the same range.
The results of evaluation of artificial organoleptic properties of the ultrafiltrate fraction P2 and the chromatographs fractions F1-F4 are given in the following table.
TABLE 1 sensory evaluation results
As can be seen from the results in Table 1, the flavor profiles of the chromatographic fraction F4 and the membrane separation fraction P2 are most similar, and the umami taste is more distinct and the taste is rich.
In order to further determine the taste of each component, sensory analysis was performed by using the interaction of chicken soup and flavor peptide using a 5-point scale method. Sensory evaluation score 0 indicated no taste, and 5 indicated that the richness was the most intense. When the taste of the flavor development peptide is subjected to strong sensory evaluation, the temperature of the sample is maintained at 40 +/-2 ℃.
Preparing 0.2g/L solution of each chromatographic component F1-F6, adding 10ml of each chromatographic component into 50ml of chicken soup reference solution to prepare sample solution, and adding 10ml of deionized water into the pure chicken soup reference solution to serve as blank control. The chicken soup reference solution is prepared by using stewed chicken soup thick soup treasure purchased from union lihua company, diluting with 1000ml deionized water per 128g thick soup treasure, and sealing for later use. The scoring results are shown in fig. 3.
Combining the results of FIGS. 1-3 and Table 1, it can be considered that: the component F4 has the most delicious taste and the most intense taste, so that the component F4 is selected for the next RP-HPLC separation and purification.
And (4): further separating and purifying F4 component
Further separation and purification of the F4 fraction were carried out by RP-HPLC. The column used was Spursil C18(5 μm, 250 x 4.6 mm; Dikma Technologies Inc.). The RP-HPLC separation conditions were: isocratic elution, 30% methanol and 70% ultrapure water, flow rate: 0.8mL/min, column temperature: the sample loading was 10. mu.L at 25 ℃ and the detection wavelength was 220 nm.
The RP-HPLC separation spectrum of chromatography component F4 is shown in FIG. 4. In the figure, the abscissa represents elution time (min), and the ordinate represents abundance at a detection wavelength of 220 nm.
From the three absorption peaks seen in fig. 4, the absorption peaks of the elution were collected to give 3 separated fractions (designated as F4a, F4b, F4c in this order). The components are freeze-dried and stored at-80 ℃.
And (5): the taste characteristics of the RP-HPLC separated fractions were analyzed using artificial sensory evaluation analysis.
Sensory evaluation was performed by 8 sensory evaluators (4 men and 4 women, age 25 to 30 years). And (4) training the evaluator according to the training method in the step (3). Sensory samples were prepared on a 5-point scale. RP-HPLC components F4a, F4b and F4c are prepared into 0.2g/L solution, 10ml of each component is added into 50ml of chicken soup reference solution respectively to prepare sample solution. A blank was prepared by adding 50ml of chicken broth to 10ml of deionized water. Evaluation was performed by a sensory evaluator. Sensory evaluation score 0 indicated no taste, 5 indicated that the richness was the most intense, and the sample temperature was evaluated at 40 ± 2 ℃. The sensory evaluation results are shown in fig. 5.
As can be seen in FIG. 5, component F4b was the most potent in taste, and therefore F4b was selected for polypeptide sequence identification.
Step (6) identification of polypeptide sequence Structure of component F4b
Preparing a sample: dissolving the F4 component sample in chromatographic pure water, mixing on a vortex mixer to fully dissolve the component, and centrifuging to obtain a supernatant for later use.
The UPLC-Q-TOF-MS measurement conditions are as follows:
liquid phase conditions: a BEH C18 column (5 cm. times.2.1 mm, 1.7 μm) was used: the sample volume is 10 mu L; flow rate: 0.3 ml/min; gradient elution is carried out by adopting two kinds of eluent as mobile phases, wherein the eluent A is 0.1% acetonitrile water solution, and the eluent B is 0.1% formic acid water solution; the column temperature is 45 ℃; the gradient elution conditions were as follows: 0-2 min: 100% of B; 2-3 min: 90% of B; 3-10 min: 0% of B.
The mass spectrometry conditions were as follows: ionization mode: ESI +, capillary voltage of 3.2Kvolts, cone hole voltage of 20Kvolts, ion source temperature of 100 ℃, desolvation vaporization temperature of 400 ℃, cone hole flow rate of 50L/h, ion energy of 1Volt, collision energy of 6Volts and 20Volts, scanning time of 1s, detection voltage of 1700Volts, and mass range of 20-1000 m/z.
After separation and identification of component F4b by UPLC-Q-TOF-MS, the relative molecular weight of the separated component F4b was identified by Biolynx in Masslynx. The abscissa of FIG. 6 is the molecular weight (m/z) and the ordinate represents the abundance. The result from FIG. 6 shows the major ionic fragment ([ M + ] of F4bH] + ) 505.8, and finally a relative molecular mass of 503.99 Da. The amino acid sequence of the F4b fraction was identified by secondary mass spectrometry and analyzed to give the final peptide sequence Gly-Val-Gly-Ala-Pro, the results are shown in FIG. 7. The abscissa of fig. 7 is the molecular weight (m/z) of the ion fragment and the ordinate is the abundance.
In conclusion, the polypeptide sequence structure of the flavor peptide of the RP-HPLC separation component F4b can be obtained, and the amino acid sequence is shown in SEQ ID NO. 1.
And (7) preparing the hypsizygus marmoreus Maillard peptide.
Dissolving the obtained flavor development peptide of the beech mushroom with water to prepare a 20% peptide solution, adding xylose according to the ratio of 3:1 of the peptide to the sugar, uniformly mixing, adjusting the pH value to 8.0 by using 1% citric acid and 5% sodium citrate solution, reacting for 3h at the temperature of 120 ℃, and cooling by using ice water to terminate the reaction. Sensory evaluation results show that the flavor development peptide of the hypsizygus marmoreus has stronger delicate flavor and thick taste after undergoing the Maillard reaction. The hypsizygus marmoreus flavor-developing peptide in the embodiment has an obvious flavor enhancement effect, can be used in the field of foods, can be used as a base material and an auxiliary material to be added with seasonings, and enriches the taste of the foods.
SEQUENCE LISTING
<110> Shanghai applied technology university
<120> Hypsizygus marmoreus flavor-developing peptide and preparation method and application thereof
<130> BCN1191681
<160> 1
<170> PatentIn version 3.5
<210> 1
<211> 5
<212> PRT
<213> Artificial sequence
<400> 1
Gly Val Gly Ala Pro
1 5
Claims (2)
1. The application of the hypsizygus marmoreus taste-presenting peptide in the seasoning is characterized in that the amino acid sequence of the hypsizygus marmoreus taste-presenting peptide is shown in SEQ ID NO: 1 is shown.
2. The seasoning is characterized by comprising a Hypsizygus marmoreus taste peptide, wherein the amino acid sequence of the Hypsizygus marmoreus taste peptide is shown as SEQ ID NO: 1 is shown.
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| CN111018949B (en) * | 2020-01-06 | 2021-06-18 | 上海应用技术大学 | Preparation method and application of grifola frondosa flavor-developing peptide |
| CN113651869B (en) * | 2021-07-14 | 2023-02-24 | 南京财经大学 | Umami peptide and preparation method and application thereof |
| CN114027494A (en) * | 2021-12-10 | 2022-02-11 | 上海市农业科学院 | Flavor base material and preparation method and application thereof |
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